› 1m46

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF MLC1P BOUND TO IQ4 OF MYO2P, A CLASS V MYOSIN

Released:
DOI: 10.2210/pdb1m46/pdb
PDB entry 1m46 coloured by chain, front view.
PDB entry 1m46 coloured by chain, side view.
PDB entry 1m46 coloured by chain, top view.
Source organisms:
Primary publication:
Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications.
Terrak M, Wu G, Stafford WF, Lu RC, Dominguez R
EMBO J 22 362-71 (2003)
PMID: 12554638

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-148625 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Myosin light chain 1 Chain: A
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 16.33 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53141 (Residues: 2-149; Coverage: 99%)
Gene names: G3080, MLC1, YGL106W
Structure domains: EF-hand
Myosin-2 Chain: B
Molecule details ›
Chain: B
Length: 25 amino acids
Theoretical weight: 3.09 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P19524 (Residues: 854-878; Coverage: 2%)
Gene names: CDC66, MYO2, O6167, YOR326W

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21212
Unit cell:
a: 48.504Å b: 121.504Å c: 29.082Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.239
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

7 review citations

Relating biochemistry and function in the myosin superfamily.
De La Cruz et al. (2004)
6 more

5 mentions without citation

Myosin light chains: Teaching old dogs new tricks.
Heissler et al. (2014)
4 more